Purification and Characterization of a Dipeptidase from Streptococcus cremoris Wg2
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چکیده
منابع مشابه
Purification and Characterization of a Dipeptidase from Streptococcus cremoris Wg2.
A dipeptidase was purified to homogeneity from a crude cell extract of Streptococcus cremoris Wg2 by DEAE-Sephacel column chromatography followed by preparative disc gel electrophoresis. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showed a single protein band with a molecular weight of 49,000. The dipeptidase is capable of hydrolyzing a range of dipeptides, ...
متن کاملPurification and Characterization of an Aminopeptidase from Lactococcus lactis subsp. cremoris Wg2.
An aminopeptidase was purified to homogeneity from a crude cell extract of Lactococcus lactis subsp. cremoris Wg2 by a procedure that included diethyl-aminoethane-Sephacel chromatography, phenyl-Sepharose chromatography, gel filtration, and high-performance liquid chromatography over an anion-exchange column. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showe...
متن کاملDeletion analysis of the proteinase gene of Streptococcus cremoris Wg2.
The Streptococcus cremoris Wg2 proteinase gene, cloned in S. lactis, specified a proteinase which exhibited the same specificity toward casein as did the proteinase isolated from the original host. Although the cloned gene lacked the last 130 codons, the proteinase still specifically degraded beta-casein. Deletion of the C-terminal 343 amino acids from the proteinase did not influence this spec...
متن کاملCell Wall-Associated Proteases of Streptococcus cremoris Wg2.
Two components of the proteolytic system, proteins A and B (J. Hugenholtz, F. Exterkate, and W. N. Konings, Appl. Environ. Microbiol. 48:1105-1110, 1984), have been studied in Streptococcus cremoris Wg2 by immunological methods. The components could not be separated by standard chromatography techniques because both proteins had almost identical molecular weights (about 140,000) and isoelectric...
متن کاملMechanism of Proteinase Release from Lactococcus lactis subsp. cremoris Wg2.
The procedure generally used for the isolation of extracellular, cell-associated proteinases of Lactococcus lactis species is based on the release of the proteinases by repeated incubation and washing of the cells in a Ca-free buffer. For L. lactis subsp. cremoris Wg2, as many as five incubations for 30 min at 29 degrees C are needed in order to liberate 95% of the proteinase. Proteinase releas...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1988
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.54.1.43-49.1988